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HtrA2 also called Omi is a mammalian serine protease at high temperatures and has a chaperone activity at low temperature. The full-length HtrA2 is synthesized as a precursor protein and then targeted to the mitochondria where it is matured by the removal of N-terminal 133 residues. Mature HtrA2 consists of a putative transmembrane domain; an inhibitor of apoptosis protein (IAP)-binding motif; a single C-terminal PDZ domain that mediates protein-protein interactions. Recently, HtrA2 has known to contribute both to caspase-dependent and caspase-independent cell death.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

PPP1CA is one of the 3 catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase which is involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity is detected in the end stage of heart failure. Studies in both human and mice suggest that PP1 is a significant regulator of cardiac function. Mouse studies also propose that PP1 functions as a suppressor of learning and memory.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes. MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells.
The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds.
TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer.

RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.

CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.

Cyclin-dependent kinase inhibitor 1B (CDKN1B) is a member of the Cip/Kip family of cyclin dependent kinase (Cdk) inhibitor proteins. The CDKN1B protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and so controls the cell cycle progression at G1. CDKN1B is often referred to as a cell cycle inhibitor protein since its major function is to stop or slow down the cell division cycle. The degradation of the CDKN1B protein, which is triggered by its CDK dependent phosphorylation and ensuing ubiquitination by SCF complexes, is compulsory for the cellular transition from inactive to the proliferative state.

HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells. Mutations in UMPS are the reason of inherited orotic aciduria disease.

The glucagon-like peptide-1 receptor, also known as GLP1R, is a receptor protein found on brain neurons and beta cells of the pancreas. GLP1R activates a signalling cascade that leads to the initiation of adenylyl cyclase and increased intracellular cAMP levels. In humans, GLP1R is synthesized by GLP1R gene, which is present on chromosome 6.
GLP1R takes part in the control of blood sugar level by enhancing insulin secretion. GLP1R is a part of the glucagon receptor family of G protein-coupled receptors. GLP1R consists of two domains, one transmembrane (TMD) domain, that binds the N-terminal region of GLP-1. And one extracellular (ECD) which binds the C-terminal helix of GLP-1. The TMD domain contains a fulcrum of polar residues that controls the biased signaling of the receptor, while the transmembrane helical boundaries and extracellular surface are a trigger for biased agonism.

CDKN2C is a member of the CDKN2 cyclin-dependent kinase inhibitor family. CDKN2C cooperates with CDK4 or CDK6, and inhibits the activation of the CDK kinases, therefore acts as a cell growth regulator which regulates cell cycle G1 progression. CDKN2C suppresses the cell growth and proliferation with a correlated dependency on endogenous retinoblastoma protein RB. Studies in the knockout mice show CDKN2C takes part in regulating spermatogenesis, in addition to suppressing tumorigenesis.

Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.

Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.

Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.

FARSB, also known as Phenylalanyl-TRNA Synthetase Beta is a member of the phenylalanyl-tRNA synthetase beta subunit family. FARSB is composed tetramer of two alpha and two beta subunits. In the presence of ATP, this tetramer is accountable for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA.

CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.